Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1973 Oct 1;59(1):213–222. doi: 10.1083/jcb.59.1.213

PROTEIN ABSORPTION BY RENAL CELLS

II. Very Rapid Lysosomal Digestion Of Exogenous Ribonuclease In Vitro

Samuel James Davidson 1
PMCID: PMC2110925  PMID: 4584726

Full Text

The Full Text of this article is available as a PDF (690.8 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baccino F. M., Rita G. A., Zuretti M. F. Studies on the structure-bound sedimentabolity of some rat liver lysosome hydrolases. Biochem J. 1971 Apr;122(3):363–371. doi: 10.1042/bj1220363. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bertini F., Mego J. L., McQueen J. D. Distribution in tissue homogenates, and the nature of the linkage of injected proteins to subcellular particles. J Cell Physiol. 1967 Aug;70(1):105–114. doi: 10.1002/jcp.1040700114. [DOI] [PubMed] [Google Scholar]
  3. Creemers J., Jacques P. J. Endocytic uptake and vesicular transport of injected horseradish peroxidase in the vacuolar apparatus of rat liver cells. Exp Cell Res. 1971 Jul;67(1):188–203. doi: 10.1016/0014-4827(71)90634-3. [DOI] [PubMed] [Google Scholar]
  4. Davidson S. J., Hughes W. L., Barnwell A. Renal protein absorption into sub-cellular particles. I. Studies with intact kidneys and fractionated homogenates. Exp Cell Res. 1971 Jul;67(1):171–187. doi: 10.1016/0014-4827(71)90633-1. [DOI] [PubMed] [Google Scholar]
  5. Davies M., Lloyd J. B., Beck F. Protein digestion in isolated lysosomes inhibited by intralysosomal trypan blue. Science. 1969 Mar 28;163(3874):1454–1456. doi: 10.1126/science.163.3874.1454. [DOI] [PubMed] [Google Scholar]
  6. De Duve C., Wattiaux R. Functions of lysosomes. Annu Rev Physiol. 1966;28:435–492. doi: 10.1146/annurev.ph.28.030166.002251. [DOI] [PubMed] [Google Scholar]
  7. Ehrenreich B. A., Cohn Z. A. The uptake and digestion of iodinated human serum albumin by macrophages in vitro. J Exp Med. 1967 Nov 1;126(5):941–958. doi: 10.1084/jem.126.5.941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Goettlich-Riemann W., Young J. O., Tappel A. L. Cathepsins D, A and B, and the effect of pH in the pathway of protein hydrolysis. Biochim Biophys Acta. 1971 Jul 25;243(1):137–146. doi: 10.1016/0005-2795(71)90047-x. [DOI] [PubMed] [Google Scholar]
  9. Goldfischer S., Novikoff A. B., Albala A., Biempica L. Hemoglobin uptake by rat hepatocytes and its breakdown within lysosomes. J Cell Biol. 1970 Mar;44(3):513–529. doi: 10.1083/jcb.44.3.513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Huang F. L., Tappel A. L. Action of cathepsins C and D in protein hydrolysis. Biochim Biophys Acta. 1971 Jun 29;236(3):739–748. doi: 10.1016/0005-2795(71)90259-5. [DOI] [PubMed] [Google Scholar]
  11. Jensen M. S., Bainton D. F. Temporal changes in pH within the phagocytic vacuole of the polymorphonuclear neutrophilic leukocyte. J Cell Biol. 1973 Feb;56(2):379–388. doi: 10.1083/jcb.56.2.379. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  13. MEGO J. L., MCQUEEN J. D. THE UPTAKE AND DEGRADATION OF INJECTED LABELED PROTEINS BY MOUSE-LIVER PARTICLES. Biochim Biophys Acta. 1965 Apr 12;100:136–143. doi: 10.1016/0304-4165(65)90436-8. [DOI] [PubMed] [Google Scholar]
  14. Mego J. L., Bertini F., McQueen J. D. The use of formaldehyde-treated 131-I-albumin in the study of digestive vacuoles and some properties of these particles from mouse liver. J Cell Biol. 1967 Mar;32(3):699–707. doi: 10.1083/jcb.32.3.699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Mego J. L. Heterolysosome formation and function in some Anurans. Comp Biochem Physiol B. 1971 Sep 15;40(1):263–273. doi: 10.1016/0305-0491(71)90082-4. [DOI] [PubMed] [Google Scholar]
  16. Mego J. L., McQueen J. D. Further studies on the degradation of injected [131-I] albumin by secondary lysosomes of mouse liver. Biochim Biophys Acta. 1965 Nov 15;111(1):166–173. doi: 10.1016/0304-4165(65)90483-6. [DOI] [PubMed] [Google Scholar]
  17. Mego J. L., McQueen J. D. Heterolysosome formation in mouse liver. J Cell Physiol. 1967 Aug;70(1):115–120. doi: 10.1002/jcp.1040700115. [DOI] [PubMed] [Google Scholar]
  18. Misaka E., Tappel A. L. Inhibition studies of cathepsins A, B, C and D from rat liver lysosomes. Comp Biochem Physiol B. 1971 Apr 15;38(4):651–662. doi: 10.1016/0305-0491(71)90268-9. [DOI] [PubMed] [Google Scholar]
  19. SHIBKO S., TAPPEL A. L. RAT-KIDNEY LYSOSOMES: ISOLATION AND PROPERTIES. Biochem J. 1965 Jun;95:731–741. doi: 10.1042/bj0950731. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Shibko S., Pangborn J., Tappel A. L. Studies on the release of lysosomal enzymes from kidney lysosomes. J Cell Biol. 1965 Jun;25(3):479–483. doi: 10.1083/jcb.25.3.479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Williams K. E., Lloyd J. B., Davies M., Beck F. Digestion of an exogenous protein by rat yolk-sac cultured in vitro. Biochem J. 1971 Nov;125(1):303–308. doi: 10.1042/bj1250303. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES